Kinetics studies on the lignan class of natural compounds that inhibits α-chymotrypsin

• Published in: Journal of asian natural products research Vol. 11; no. 11; pp. 933 - 939
• Main Authors: Abbasi, M.A., Lodhi, M.A., Ahmad, V.U., Choudhary, M.I.
• Format: Journal Article
• Language: English
• Published: Abingdon Taylor & Francis Group 01-11-2009; Taylor & Francis
• Subjects: Biological and medical sciences; Chymotrypsin - antagonists & inhibitors; Commiphora mukul Engl; General pharmacology; lignans; Lignans - chemistry; Lignans - isolation & purification; Lignans - pharmacokinetics; Magnoliaceae - chemistry; Mathematics; Medical sciences; Molecular Structure; Pakistan; Pharmacognosy. Homeopathy. Health food; Pharmacology. Drug treatments; Plants, Medicinal - chemistry; α-chymotrypsin inhibition; Asia; India; Oxygen heterocycle; Medicinal plant; Commiphora mukul Engl; α-chymotrypsin inhibition; Folk medicine; Dicotyledones; Angiospermae; Ayurvedic medicine; Bicyclic compound; Lignan; Aromatic compound; Serine endopeptidases; Ether; Enzyme; Pharmacognosy; Enzyme inhibitor; Natural compound; Burseraceae; In vitro; Biological activity; lignans; Peptidases; Chymotrypsin; Plant origin; Hydrolases; Non competitive inhibition; Spermatophyta; Kinetics
• ISSN: 1028-6020; 1477-2213
• DOI: 10.1080/10286020903321539

The mechanism of inhibition of the α-chymotrypsin enzyme by two lignans of the fused bistetrahydrofuran series, epiexcelsin (1) and 5′-demethoxyepiexcelsin (2), which were isolated from the Commiphora mukul Engl., was investigated. Lineweaver-Burk and Dixon plots and their secondary replots showed that these compounds were noncompetitive inhibitors of the enzyme. K
i
values for 1 and 2 were found to be 22.29 ± 0.015 and 336.30 ± 0.053 μM, respectively.